Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3

ADP−Fluoroaluminate Complexes Are Formed

ADP−Fluoroaluminate Complexes Are Formed Cooperatively at Two Catalytic Sites of Wild-Type and Mutant α 3 β 3 γ Subcomplexes of the F 1 -ATPase from the Thermophilic Bacillus PS3 †

✍ Dou, Chao; Grodsky, Neil B.; Matsui, Tadashi; Yoshida, Masasuke; Allison, Willia 📂 Article 📅 1997 🏛 American Chemical Society 🌐 English ⚖ 216 KB

The βG 156 C Substitution in the F 1 -AT

The βG 156 C Substitution in the F 1 -ATPase from the Thermophilic Bacillus PS3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site †

✍ Bandyopadhyay, Sanjay; Valder, Carolina R.; Huynh, Hue G.; Ren, Huimiao; Allison 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 170 KB

Mutations in the Nucleotide Binding Doma

Mutations in the Nucleotide Binding Domain of the α Subunits of the F 1 -ATPase from Thermophilic Bacillus PS3 That Affect Cross-Talk between Nucleotide Binding Sites †

✍ Grodsky, Neil B.; Dou, Chao; Allison, William S. 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 176 KB

The .alpha.3.beta.3.gamma. complex of th

The .alpha.3.beta.3.gamma. complex of the F1-ATPase from thermophilic Bacillus PS3 containing the .alpha.D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites

✍ Jault, Jean-Michel; Matsui, Tadashi; Jault, Francoise M.; Kaibara, Chitose; Mune 📂 Article 📅 1995 🏛 American Chemical Society 🌐 English ⚖ 891 KB

The .alpha.3.beta.3.gamma. complex of th

The .alpha.3.beta.3.gamma. complex of the F1-ATPase from thermophilic Bacillus PS3 containing the .alpha.D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites

✍ Jault, Jean-Michel; Matsui, Tadashi; Jault, Francoise M.; Kaibara, Chitose; Mune 📂 Article 📅 1995 🏛 American Chemical Society 🌐 English ⚖ 891 KB

ATP hydrolyses by the wild-type a&y and mutant (aD261N)3P3y subcomplexes of the FI-ATPase from the thermophilic Bacillus PS3 have been compared. The wild-type complex hydrolyzes 50 p M ATP in three kinetic phases: a burst decelerates to an intermediate phase, which then gradually accelerates to a fi

The α 3 (βY 341 W) 3 γ Subcomplex of the

The α 3 (βY 341 W) 3 γ Subcomplex of the F 1 -ATPase from the Thermophilic Bacillus PS3 Fails to Dissociate ADP When MgATP Is Hydrolyzed at a Single Catalytic Site and Attains Maximal Velocity When Three Catalytic Sites Are Saturated with MgATP †

✍ Dou, Chao; Fortes, P. A. George; Allison, William S. 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 164 KB